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Literature summary for 3.2.1.1 extracted from
- Cloning and extracellular expression of a raw starch digesting alpha-amylase (Blamy-I) and its application in bioethanol production from a non-conventional source of starch (2015), J. Basic Microbiol., 55, 1287-1298 .
Application
| Application | Comment | Organism |
|---|---|---|
| biofuel production | the recombinant enzyme can be utilized for bioethanol production from jackfruit seed starch | Bacillus licheniformis |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene amyA, sequence comparisons, recombinant overexpression in Escherichia coli strain BL21 (DE3) using the native signal peptide, method optimization leading to 8fold increased production of extracellular enzyme. The amylase activity in culture supernatant of Escherichia coli cells from non-optimized conditions is 51.2 U/ml, from optimized conditions 409.5 U/ml | Bacillus licheniformis |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 4-bromophenacyl bromide | - |
Bacillus licheniformis |  |
| EDTA | - |
Bacillus licheniformis | |
| Hg2+ | - |
Bacillus licheniformis | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Lineweaver-Burk kinetics, Km for raw starch from jackfruit is 5.56 mg/ml | Bacillus licheniformis |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| extracellular | - |
Bacillus licheniformis | - |
- |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | presence of an extra Ca2+-binding region between the A and C domains responsible for higher thermostability of this enzyme | Bacillus licheniformis | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 55000 | - |
recombinant enzyme, native PAGE | Bacillus licheniformis |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus licheniformis | I3P686 | - |
- |
| Bacillus licheniformis AS08E | I3P686 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant extracellular enzyme 14.2fold from Escherichia coli strain BL21 (DE3) by hydrophobic interaction chromatography and gel filtration to homogeneity | Bacillus licheniformis |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
amylase activity in culture supernatant of Escherichia coli cells from non-optimized conditions is 51.2 U/ml, from optimized conditions 409.5 U/ml | Bacillus licheniformis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| raw starch + H2O | hydrolyzed raw starch isolated from a jack fruit seed cotyledons, recombinant enzyme can hydrolyze raw jackfruit seed starch up to 52% after 6 h treatment at 30°C | Bacillus licheniformis | maltose + maltotriose | - |
? | |
| raw starch + H2O | hydrolyzed raw starch isolated from a jack fruit seed cotyledons, recombinant enzyme can hydrolyze raw jackfruit seed starch up to 52% after 6 h treatment at 30°C | Bacillus licheniformis AS08E | maltose + maltotriose | - |
? | |
| soluble starch + H2O | - |
Bacillus licheniformis | maltose + maltotriose | - |
? | |
| soluble starch + H2O | - |
Bacillus licheniformis AS08E | maltose + maltotriose | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| monomer | 1 * 55300, recombinant enzyme, SDS-PAGE | Bacillus licheniformis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| AmyA | - |
Bacillus licheniformis |
| Blamy-I | - |
Bacillus licheniformis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 80 | - |
recombinant extracellular enzyme Blamy-I | Bacillus licheniformis |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 60 | 70 | recombinant enzyme, stable up to in absence of Ca2+ | Bacillus licheniformis |
| 80 | - |
recombinant enzyme, stable up to in presence of Ca2+ | Bacillus licheniformis |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 10 | - |
recombinant extracellular enzyme Blamy-I | Bacillus licheniformis |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 6 | 12 | recombinant enzyme, stable at | Bacillus licheniformis |
pI Value
| Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|
| Bacillus licheniformis | sequence calculation | - |
6.05 |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | structure-function analysis of recombinant enzyme Blamy-I, homology modeling of the three-dimensional structure of Blamy-I using the X-ray crystallography structure of alpha-amylase, PDB ID 1ob0A, as the template | Bacillus licheniformis |
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